新型阿片肽α-新内啡肽化学合成基因在大肠杆菌中的表达
Expression in Escherichia coli of chemically synthesized gene for a novel opiate peptide alpha-neo-endorphin.
作者信息
Tanaka S, Oshima T, Ohsue K, Ono T, Oikawa S, Takano I, Noguchi T, Kangawa K, Minamino N, Matsuo H
出版信息
Nucleic Acids Res. 1982 Mar 11;10(5):1741-54. doi: 10.1093/nar/10.5.1741.
Abstract
Chemically synthesized alpha-neo-endorphin gene was fused to the Escherichia coli beta-galactosidase gene on the plasmid pKO13. The resulting recombinant DNA was used to transform E. coli cells. Radioimmunoassay for alpha-neo-endorphin in CNBr-treated bacterial cells showed that alpha-neo-endorphin was synthesized at approximately 5 x 10(5) molecules per single E. coli cell. One of the transformants, WA802/p alpha NE2, was used for alpha-neo-endorphin purification. From 10.9 g of wet cells, we isolated 4 mg of chemically pure and biologically active alpha-neo-endorphin.
摘要
将化学合成的α-新内啡肽基因与质粒pKO13上的大肠杆菌β-半乳糖苷酶基因融合。所得重组DNA用于转化大肠杆菌细胞。对经溴化氰处理的细菌细胞中的α-新内啡肽进行放射免疫测定表明，每个大肠杆菌细胞约合成5×10⁵个α-新内啡肽分子。其中一个转化体WA802/pαNE2用于α-新内啡肽的纯化。从10.9克湿细胞中，我们分离出4毫克化学纯且具有生物活性的α-新内啡肽。
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